Structure of PDB 1m9h Chain A

Receptor sequence
>1m9hA (length=277) Species: 1720 (Corynebacterium sp.) [Search protein sequence]
TVPSIVLNDGNSIPQLGYGVYKVPPADTQRAVEEALEVGYRHIDTAAIYG
NEEGVGAAIAASGIARDDLFITTKLWNDRHDGDEPAAAIAESLAKLALDQ
VDLYLVHWPTPAADNYVHAWEKMIELRAAGLTRSIGVSNHLVPHLERIVA
ATGVVPAVNQIELHPAYQQREITDWAAAHDVKIESWGPLGQGKYDLFGAE
PVTAAAAAHGKTPAQAVLRWHLQKGFVVFPGSVRREHLEENLDVFDFDLT
DTEIAAIDAMDPGDGSGRVSGHPDEVD
3D structure
PDB1m9h Structural alteration of cofactor specificity in Corynebacterium 2,5-diketo-D-gluconic acid reductase
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D45 Y50 K75 H108
Catalytic site (residue number reindexed from 1) D44 Y49 K74 H107
Enzyme Commision number 1.1.1.346: 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming).
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 NAD A G20 Y22 Y50 H108 Q161 W187 G188 P189 L190 Q192 A215 F230 P231 G232 H238 N242 G19 Y21 Y49 H107 Q160 W186 G187 P188 L189 Q191 A214 F229 P230 G231 H237 N241
Gene Ontology
Molecular Function
GO:0016491 oxidoreductase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Biological Process
GO:0019853 L-ascorbic acid biosynthetic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1m9h, PDBe:1m9h, PDBj:1m9h
PDBsum1m9h
PubMed14718658
UniProtP06632|DKGA_CORSC 2,5-diketo-D-gluconic acid reductase A (Gene Name=dkgA)

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